Proteomic and amino acid profiling of monofloral honeys from the Thrace region: insights into composition

This study conducted a comprehensive proteomic and amino acid analysis of five monofloral honeys from the Thrace region: sunflower (Helianthus annuus), oak (Quercus), Christ's thorn (Paliurus spina-christi), bindweed (Convolvulus), and goosefoot (Chenopodium album). The combined use of reverse-phase and normal-phase (HILIC) LC-QTOF methods led to the identification of 39 bee-derived proteins, nine of which (including phospholipase A1 and carboxylic ester hydrolase) were common to all honeys. Plant-derived proteins were found to be most abundant in sunflower honey. NanoDrop quantification revealed protein contents ranging from 0.2% to 0.4%, with Christ's thorn honey exhibiting the highest concentration. Free amino acid profiling via LC–MS/MS identified proline as the predominant amino acid, occurring at very high levels, particularly in Christ's thorn honey (10.184 nmol/g). The findings underscore the potential of monofloral honeys for cosmetic applications (e.g., anti-aging formulations) and as dietary supplements. Furthermore, the results suggest that proteomic analysis may serve as an effective method for authenticity testing to combat honey adulteration. This research is focused on the detailed accountability of cutting room wastages with respect to four categories that is, splice loss, remnant loss, buffer loss and width loss Comprehensive proteomic and amino acid analysis of five monofloral honeys from the Thrace region. Identification of 39 bee-derived proteins, with nine common across all honeys. Christ's thorn honey exhibited the highest protein and proline content. Potential applications in cosmetics (anti-aging formulations) and dietary supplements. Proteomics may be an effective method for honey authenticity testing.